Abstract
In order to purify honeysuckle peroxides and study the enzymatic properties and inhibition kinetics,DEAE cellulose DE-52 ion exchange chromatography was used for purification of peroxidase from Lonicera Japonica Thunb prepared preliminarily by three-phase partitioning. Two kinds of peroxidase, HSPⅠ(honeysuckle peroxidaseⅠ)and HSPⅡ(honeysuckle peroxidaseⅡ), were purified,the specific activity were 3 312.3 U/mg and 564.8 U/mg respectively. The double substrate enzymatic reaction type was PingPong reaction analyzed by the reaction kinetics. Citric acid, Sodium metabisulfite showed irreversible inhibition to Lonicera Japonica Thunb peroxidase, L-cysteine showed reversible inhibition, and L-cysteine was a competitive inhibitor that the inhibition constant KI was 0.053 mmol/L.
Publication Date
7-28-2017
First Page
111
Last Page
116
DOI
10.13652/j.issn.1003-5788.2017.07.026
Recommended Citation
Lei, LUO; Jinlong, DONG; Wenxue, ZHU; and Yihan, XUE
(2017)
"Study on inhibition kinetics of peroxidase from Lonicera Japonica Thunb,"
Food and Machinery: Vol. 33:
Iss.
7, Article 26.
DOI: 10.13652/j.issn.1003-5788.2017.07.026
Available at:
https://www.ifoodmm.cn/journal/vol33/iss7/26
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